| D010100 |
Oxygen |
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration. |
Dioxygen,Oxygen-16,Oxygen 16 |
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| D002460 |
Cell Line |
Established cell cultures that have the potential to propagate indefinitely. |
Cell Lines,Line, Cell,Lines, Cell |
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| D002470 |
Cell Survival |
The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability. |
Cell Viability,Cell Viabilities,Survival, Cell,Viabilities, Cell,Viability, Cell |
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| D000072224 |
Bcl-2-Like Protein 11 |
A BCL-2-like protein that has a C-terminal BCL-2 homology (BH3) domain and forms heterodimers with other BCL-2 FAMILY PROTEINS. It is a strong inducer of APOPTOSIS and ANOIKIS; several isoforms are expressed (BimEL, Bim L, Bim-alpha, Bim-s; and Bim-gamma) that have different potencies for inducing apoptosis. |
BCL2L11 Protein,BIM Protein,Bcl-2-Binding Protein, BIM,Bcl-2-Interacting Mediator of Cell Death,11, Bcl-2-Like Protein,BIM Bcl-2-Binding Protein,Bcl 2 Binding Protein, BIM,Bcl 2 Interacting Mediator of Cell Death,Bcl 2 Like Protein 11,Protein 11, Bcl-2-Like,Protein, BCL2L11,Protein, BIM,Protein, BIM Bcl-2-Binding |
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| D000818 |
Animals |
Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. |
Animal,Metazoa,Animalia |
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| D015536 |
Down-Regulation |
A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins. |
Receptor Down-Regulation,Down-Regulation (Physiology),Downregulation,Down Regulation,Down-Regulation, Receptor |
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| D015687 |
Cell Hypoxia |
A condition of decreased oxygen content at the cellular level. |
Anoxia, Cellular,Cell Anoxia,Hypoxia, Cellular,Anoxia, Cell,Anoxias, Cell,Anoxias, Cellular,Cell Anoxias,Cell Hypoxias,Cellular Anoxia,Cellular Anoxias,Cellular Hypoxia,Cellular Hypoxias,Hypoxia, Cell,Hypoxias, Cell,Hypoxias, Cellular |
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| D017209 |
Apoptosis |
A regulated cell death mechanism characterized by distinctive morphologic changes in the nucleus and cytoplasm, including the endonucleolytic cleavage of genomic DNA, at regularly spaced, internucleosomal sites, i.e., DNA FRAGMENTATION. It is genetically programmed and serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth. |
Apoptosis, Extrinsic Pathway,Apoptosis, Intrinsic Pathway,Caspase-Dependent Apoptosis,Classic Apoptosis,Classical Apoptosis,Programmed Cell Death,Programmed Cell Death, Type I,Apoptoses, Extrinsic Pathway,Apoptoses, Intrinsic Pathway,Apoptosis, Caspase-Dependent,Apoptosis, Classic,Apoptosis, Classical,Caspase Dependent Apoptosis,Cell Death, Programmed,Classic Apoptoses,Extrinsic Pathway Apoptoses,Extrinsic Pathway Apoptosis,Intrinsic Pathway Apoptoses,Intrinsic Pathway Apoptosis |
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| D017346 |
Protein Serine-Threonine Kinases |
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors. |
Protein-Serine-Threonine Kinases,Serine-Threonine Protein Kinase,Serine-Threonine Protein Kinases,Protein-Serine Kinase,Protein-Serine-Threonine Kinase,Protein-Threonine Kinase,Serine Kinase,Serine-Threonine Kinase,Serine-Threonine Kinases,Threonine Kinase,Kinase, Protein-Serine,Kinase, Protein-Serine-Threonine,Kinase, Protein-Threonine,Kinase, Serine-Threonine,Kinases, Protein Serine-Threonine,Kinases, Protein-Serine-Threonine,Kinases, Serine-Threonine,Protein Kinase, Serine-Threonine,Protein Kinases, Serine-Threonine,Protein Serine Kinase,Protein Serine Threonine Kinase,Protein Serine Threonine Kinases,Protein Threonine Kinase,Serine Threonine Kinase,Serine Threonine Kinases,Serine Threonine Protein Kinase,Serine Threonine Protein Kinases |
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| D017354 |
Point Mutation |
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair. |
Mutation, Point,Mutations, Point,Point Mutations |
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